Open AccessSolution Conformation of Virginiamycins (Staphylomycins)
Author(s) -
ANTEUNIS Marc J. O.,
CALLENS Roland E. A.,
TAVERNIER Dirk K.
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02371.x
Subject(s) - orientation (vector space) , peptide bond , spectral line , crystallography , nuclear magnetic resonance , bond , chemistry , computational chemistry , peptide , physics , mathematics , geometry , quantum mechanics , finance , economics
The 1 H (at 300 MHz) and 13 C nuclear magnetic resonance spectra of virginiamycins S and S 4 and vernamycin Bα have been unravelled and analyzed. Together with model building and theoretical considerations, this allows the detailed description of their solution conformations. The depside bond can rotate and gives to the backbone some conformational mobility. The orientation of the depsicarbonyl bond depends on the surrounding. Apparent discrepancies between the different methods that are applicable for the disclosure of the nature of peptide H‐bonding, have found a rational explanation.